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Related Concept Videos

Peptide Bonds02:43

Peptide Bonds

A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
Preparation of Amides01:29

Preparation of Amides

Amides are synthesized by treating carboxylic acids with amines in the presence of dehydrating agents like dicyclohexylcarbodiimide (DCC).
The DCC-promoted synthesis of amides begins with the protonation of DCC by carboxylic acid. The protonation makes it a better acceptor. Next, the addition of carboxylate to the protonated carbodiimide gives a reactive acylating agent.
Subsequently, the amine acts as a nucleophile that attacks the acylating agent to form a tetrahedral intermediate. In the...
Amino acids03:42

Amino acids

Amino acids are the monomers that comprise proteins. Each amino acid has the same fundamental structure, which consists of a central carbon atom, or the alpha (α) carbon, bonded to an amino group (NH2), a carboxyl group (COOH), and to a hydrogen atom. Every amino acid also has another atom or group of atoms bonded to the central atom known as the R group. There are 20 common amino acids present in proteins, each with a different R group. Variation in the amino acid sequence is responsible for...
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...

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Constructing Cyclic Peptides Using an On-Tether Sulfonium Center
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Published on: September 28, 2022

Efficient peptide coupling involving sterically hindered amino acids.

Alan R Katritzky1, Ekaterina Todadze, Parul Angrish

  • 1Center for Heterocyclic Compounds, Department of Chemistry, University of Florida, Gainesville, FL 32611-7200, USA. katritzky@chem.ufl.edu

The Journal of Organic Chemistry
|June 22, 2007
PubMed
Summary

This study introduces a new method for synthesizing sterically hindered peptides using benzotriazole activation. This approach successfully incorporates hindered amino acids while maintaining complete chirality, offering a novel route for peptide synthesis.

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Area of Science:

  • Organic Chemistry
  • Peptide Synthesis
  • Medicinal Chemistry

Background:

  • Sterically hindered amino acids are challenging to incorporate into peptide chains.
  • Existing peptide synthesis methods often struggle with hindered residues, impacting peptide structure and function.
  • Developing efficient methods for hindered peptide synthesis is crucial for drug discovery and biomaterials.

Purpose of the Study:

  • To develop a novel and efficient method for synthesizing sterically hindered peptides.
  • To demonstrate the utility of N-(Cbz- and Fmoc-alpha-aminoacyl)benzotriazoles for incorporating hindered amino acids.
  • To achieve complete retention of chirality during the synthesis of hindered peptides.

Main Methods:

  • Coupling of N-(Cbz- and Fmoc-alpha-aminoacyl)benzotriazoles with sterically hindered amino acids.
  • Utilizing benzotriazole activation methodology for peptide bond formation.
  • Analysis of synthesized compounds using Nuclear Magnetic Resonance (NMR) and High-Performance Liquid Chromatography (HPLC) to confirm structure and chirality.

Main Results:

  • Successful synthesis of various sterically hindered peptide compounds (3a-e, 5a-d, 6a-c, 8a-c, 9a-e, 10a-d).
  • Isolated yields ranging from 41-95% were achieved.
  • Complete retention of chirality was confirmed by NMR and HPLC analysis, with diastereomeric mixtures also characterized.

Conclusions:

  • Benzotriazole activation provides a new and effective route for the synthesis of sterically hindered peptides.
  • The method allows for the incorporation of hindered amino acids with high efficiency and complete stereochemical control.
  • This methodology opens new possibilities for creating complex peptides with specific structural and functional properties.